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Biomedical subjects

G Marhaug

Publications and source records attributed to G Marhaug.

52 records · Page 3Linked to original sources
PubMed1985

Fragments of IgE antibodies in human feces.

The gel filtration profile of immunoglobulin E (IgE) in extracts of feces from 2 children was compared with IgE myeloma protein which had been exposed to proteolytic digestion by chymotrypsin. The peak of the chymotrypsin-digested IgE myeloma protein was found to be similar to that of fecal IgE after an elution volume between those of albumin and myoglobin, corresponding to a molecular weight of approximately 40,000 daltons. In the fractions where the peak of fecal IgE was found, no evidence for the presence of specific IgE antibodies (measured by RAST) could be detected. Fecal IgE could be purified by using an immunosorbent column to which rabbit antihuman IgE was coupled. Sufficient amounts of fecal IgE could thus be obtained and used in autoradiographic experiments. The IgE-containing fractions could also be detected with 125I-labelled second antibodies to visualize the IgE precipitates.

Antibodies↗
PubMed1985

The amyloid in familial amyloid cardiomyopathy of Danish origin is related to pre-albumin.

Amyloid obtained from the myocardium of a patient (Han) with familial amyloid cardiomyopathy of Danish origin was studied. Gel filtration and electrophoresis of purified and denatured amyloid fibrils Han revealed various fractions ranging in mol. wt from 40,000 to 8,000 daltons. Amyloid Han and fractions reacted with an antiserum against amyloid Han showing a reaction of identity with each other; partial identity between Han and human pre-albumin was observed, while no reaction was seen with AA or AL proteins. Cardiac tissue sections from Han showed reactivity with antisera to amyloid Han, pre-albumin and protein AP, but not with anti-AA or anti-AL in indirect immunofluorescence. Amino acid composition and sequence studies of a protein fraction of amyloid Han with mol. wt 15,000 daltons confirmed the structural relationship with pre-albumin.

Adult↗
PubMed1984

A comparative study of serum amyloid a protein (SAA) from mink and man.

Serum amyloid A protein (SAA) was isolated from mink and human serum by ultra-centrifugation and gel filtration and characterized by two-dimensional gel electrophoresis and Western blotting followed by autoradiography. SAA was found in similar quantities in the high density lipoprotein (HDL) fraction of serum from a patient suffering from systemic juvenile rheumatoid arthritis (JRA) and mink stimulated with lipopolysaccharide (LPS). Only very small quantities were present in normal human controls and not detectable in normal mink. Striking similarities were found in molecular weight, isoelectric point and degree of heterogeneity for human and mink SAA, while immunologic cross-reactivity between the two species was not found. In contrast to human HDL, mink HDL was found not to contain apoA-II and only minute amounts of apoC proteins.

Amyloid↗
PubMed1984

Immunoglobulin E in extracts of feces from children.

Immunoglobulin E (IgE) was demonstrated by a double antibody radioimmunoassay technique (PRIST) in 5 of 17 unconcentrated fecal extracts from children. Four of the PRIST-positive extracts also had measurable levels of IgE determined by an enzyme-linked immunosorbent test (Enzygnost IgE). However, using a competitive antibody radioimmunoassay technique (RIST), IgE was found in all unconcentrated fecal extracts. The RIST-IgE levels of the extracts were higher and did not correlate to IgE measured by the other methods, nor to the IgE in serum from the same children or to the manifestation of allergy. On the other hand, 4 of the 5 children with measurable PRIST-IgE levels, and 3 of the 4 children with detectable Enzygnost IgE concentrations in the extracts, had elevated serum IgE as well as a history of allergy. Gel filtration studies indicated that IgE determined by the PRIST and Enzygnost IgE methods had been degraded to fragments of lower molecular weight than that of albumin. This study also suggests that the IgE in feces measured by the RIST method is overestimated due to the influence from nonspecific substances of high molecular weight.

Child↗
PubMed1983

Three assays for the characterization and quantitation of human serum amyloid A.

Two different radioimmunoassays (RIA) and an enzyme-linked immunosorbent assay (ELISA) were developed for the quantitation and antigenic characterization of amyloid A (AA) and serum amyloid A (SAA) proteins, and the three assays were evaluated and compared with each other. Sensitivity, reproducibility, effect of denaturation and storage of serum and range of determination were considered. All three assays were found useful, but for different purposes. The most suitable method for the determination of SAA in whole serum was a second antibody precipitation RIA with purified SAA as labelled tracer and standard, and polyclonal rabbit anti-SAA as first antibody. This assay provided SAA concentrations in absolute amounts (mg/l) and acceptable reproducibility without need for prior denaturation of serum. Both advantages and disadvantages of ELISA using monoclonal antibodies to SAA and a solid-phase RIA using AA, SAA, anti-AA and anti-SAA were observed. The three assays were found suitable for antigenic studies of AA and SAA.

Amyloid↗
PubMed1983

Amyloid-related serum protein (SAA) as an indicator of lung infection in cystic fibrosis.

Amyloid-related serum protein (SAA) was analysed by radioimmunoassay in 32 patients with cystic fibrosis, and compared with other acute phase reactants and lung function. The level of SAA showed significant correlation with impaired lung function due to active Pseudomonas aeruginosa infection, and also to C-reactive protein. SAA seemed to correlate better to the presence of bacteria in sputum than C-reactive protein. Ten of the patients received extensive antibiotic treatment for their pulmonary infection, and falling serum levels of SAA paralleled the clinical response to treatment. Thus the concentration of SAA in these patients was a valuable guide for the selection of patients for antibiotic treatment as well as a good parameter of the response to therapy.

Adolescent↗
PubMed1983

The covalent structure of amyloid-related serum protein SAA from two patients with inflammatory disease.

The complete covalent structure of an amyloid-related serum protein SAA from a patient (Jen.) with severe rheumatoid arthritis, is presented. The structure was elucidated by N-terminal analyses of the protein as well as on peptides derived from tryptic digestion and after cleaving the protein with BNPS-skatole. The characterization of tryptic peptide T-9 revealed a polymorphism similar to that seen in protein AA. Structural studies performed on another protein SAA, isolated from a patient (Mik.) with acute systemic lupus erythematosus, indicated that this protein is homologous to that from patient Jen. The formation and deposition of the protein AA-containing amyloid fibrils is discussed.

Amino Acid Sequence↗
PubMed1983

Comparative studies of the high molecular weight amyloid fibril proteins and similar components from normal tissues.

Analysis of purified amyloid fibrils by gel filtration, polyacrylamide gel electrophoresis in SDS and 8 M urea, and immunodiffusion and immunoelectrophoresis showed that, in addition to the specific amyloid proteins AA and AL, the amyloid preparations all contain a high molecular weight complex. The latter protein complex contains fibronectin, a component which reacts with a non-AA specificity of an antiserum to degraded AA amyloid fibrils (termed the 'B' specificity), and a high molecular weight component excluded by a Sepharose 2BCL column. Similar components were found in aqueous extracts of normal tissues prepared by an identical procedure, and these form aggregates of different size in non-dissociating conditions. It is suggested that amyloid fibrils are complexes of a variety of macromolecules in addition to the specific proteins AA and AL.

Amyloid↗
PubMed1982

Amyloid A in systemic amyloidosis associated with cancer.

Amyloid fibrils from two cases of cancer-associated, systemic amyloidosis with renal cell carcinoma and mesothelioma as the respective underlying disorders were studied. The immunochemical studies suggested strongly that amyloid A comprised a principal fibril component in both cases of cancer-associated amyloidosis. This was definitively proven by amino acid sequence analyses, which revealed structural homology between a purified subcomponent of the amyloid fibrils from both of the two cases of cancer-associated amyloidosis and previously sequenced amyloid A proteins. The chemical composition of the amyloid fibrils from systemic amyloidosis associated with cancer thus corresponded to that seen in amyloidosis reactive to inflammatory diseases and Hodgkin's disease. Amyloid proteins of immunoglobulin light chain type, which are found associated with myelomatosis, macroglobulinemia, and idiopathic (primary) amyloidosis, were not found in the two amyloid preparations. Renal cell carcinoma appears to be an effective stimulator of amyloid formation, while only one case of amyloidosis associated with mesothelioma has been reported previously.

Adolescent↗
PubMed1982

Characterization of amyloid related protein SAA complexed with serum lipoproteins (apoSAA).

The amyloid related protein SAA was isolated from the serum lipoproteins of three patients with connective tissue disease, one of them having amyloidosis, and from a pool of normal control sera. The bulk of SAA (apoSAA) was complexed to high density lipoprotein (HDL), but significant amounts of apoSAA were also detected in the other lipoprotein fractions. Electrofocusing revealed five-six subspecies of SAA which were distributed in similar proportions in HDL and LDL. Three of these SAA subspecies made up almost all of the apoSAA present in HDL and LDL in the sera from the patients as well as in the control. A small portion of SAA not complexed to lipoproteins was isolated corresponding to a molecular weight higher than 200,000. No particular 'amyloid prone' SAA was found in serum from the patient with amyloidosis.

Amino Acids↗
PubMed1982

Monoclonal hybridoma antibodies to human amyloid related protein SAA.

Problems concerning isolation and characterization of the amyloid related serum protein SAA in a pure form prompted us to make monoclonal antibodies to the protein. Protein SAA isolated by gel filtration under dissociating conditions was used for immunization of BALB/c mice, and spleen cells from a mouse producing high titred antiserum to SAA were fused with cells from the mouse plasmacytoma line P3U1. Antibody specificity to various preparations of protein SAA was tested using an indirect enzyme-linked immunosorbent assay. Monoclonal antibodies with specificity for SAA were obtained in addition to antibodies which reacted with both SAA and the related amyloid protein AA. Antibodies specific for one of the apoC proteins of the lipoprotein fraction were also produced showing that the SAA preparation used for immunization was contaminated with apoC proteins.

Amyloid↗
PubMed1981

Scoliosis in children with juvenile rheumatoid arthritis.

Juvenile rheumatoid arthritis (JRA) is an unusual causative factor of scoliosis in childhood. Among 320 patients with JRA in Sweden, 17 (5.3%) had structural scoliosis of thoracic and lumbar spine. This frequency is considerably higher than in the normal population. The mean age when scoliosis was first noted was 12.4 years, corresponding to a mean duration of the JRA of 7.4 years. A curvature exceeding 20 degrees was found in 12 out of the 17 patients. The scoliosis in our patients was associated with severe and protracted polyarthritis of early onset and involvement of hip joints and cervical spine. Contracture of the hip with pelvic tilt was found in 13 and torticollis in 3 of the patients. These factors, in addition to growth disturbances and probable inflammatory processes of spinal joints, may explain the development of the scoliosis.

Adolescent↗
PubMed1981

Characterization of human amyloid-related protein SAA as a polymorphic protein: association with albumin and prealbumin in serum.

Human amyloid-related protein SAA has been prepared and purified by gel filtration, ion-exchange and affinity chromatography techniques. It was shown that SAA, even after extensive purification, is an electrophoretically heterogeneous protein. In addition, prealbumin and fragments of albumin were detected in the SAA preparation. Most of the SAA molecules and the fragments of albumin were present in a free form, but some SAA was also found to be complexed with albumin fragments.

Aged↗
PubMed1980

Effect of methotrexate on phagocytosis and killing of Staphylococcus aureus by human granulocytes.

The effect of methotrexate on the phagocytosis and killing of Staphylococcus aureus by granulocytes from healthy blood donors was investigated in vitro. A concentration of methotrexate of 2.2 x 10(-4) mol/1 (100 micrograms/ml), which is readily obtained on high dose intravenous administration did not decrease the phagocytosis and intracellular killing of Staph. aureus. In addition, granulocytes isolated from patients after termination of 6 h and 24 h high-dose methotrexate infusions showed normal phagocytic activity.

Adult↗